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. 1990 Feb 11;18(3):507–511. doi: 10.1093/nar/18.3.507

Functional implications related to the gene structure of the elongation factor EF-Tu from Halobacterium marismortui.

G Baldacci 1, F Guinet 1, J Tillit 1, G Zaccai 1, A M de Recondo 1
PMCID: PMC333455  PMID: 2155402

Abstract

The primary structure of the gene for the elongation factor EF-Tu from the halophilic archaebacterium Halobacterium marismortui (hEF-Tu) is described. It is the first gene of a halophilic elongation factor EF-Tu to be sequenced. When the sequence of hEF-Tu is compared to that of homologous proteins from other organisms, the highest identity (61%) is found with EF-Tu from Methanococcus vannielii, a non-halophilic archaebacterium. In the search for halophilic characteristics therefore the most appropriate comparison is with the M. vannielii sequence. The excess of acidic amino acid residues in the hEF-Tu sequence (already observed in the composition of other halophilic proteins) results to a large extent from changes of Lys, Asn or Gln to Asp or Glu. A structural analysis algorithm applied to the halophilic sequence places these acidic residues on the surface of the protein. The corresponding residues in the crystal structure of the first domain of EF-Tu from E. coli (the only EF-Tu structure available) are grouped in patches on the protein surface, in each of which several residues that may be far apart in the sequence come quite close to each other in the tertiary structure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. An G., Friesen J. D. The nucleotide sequence of tufB and four nearby tRNA structural genes of Escherichia coli. Gene. 1980 Dec;12(1-2):33–39. doi: 10.1016/0378-1119(80)90013-x. [DOI] [PubMed] [Google Scholar]
  2. Arai K., Clark B. F., Duffy L., Jones M. D., Kaziro Y., Laursen R. A., L'Italien J., Miller D. L., Nagarkatti S., Nakamura S. Primary structure of elongation factor Tu from Escherichia coli. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1326–1330. doi: 10.1073/pnas.77.3.1326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dever T. E., Glynias M. J., Merrick W. C. GTP-binding domain: three consensus sequence elements with distinct spacing. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1814–1818. doi: 10.1073/pnas.84.7.1814. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Frischauf A. M., Lehrach H., Poustka A., Murray N. Lambda replacement vectors carrying polylinker sequences. J Mol Biol. 1983 Nov 15;170(4):827–842. doi: 10.1016/s0022-2836(83)80190-9. [DOI] [PubMed] [Google Scholar]
  5. Gough J. A., Murray N. E. Sequence diversity among related genes for recognition of specific targets in DNA molecules. J Mol Biol. 1983 May 5;166(1):1–19. doi: 10.1016/s0022-2836(83)80047-3. [DOI] [PubMed] [Google Scholar]
  6. Guinet F., Frank R., Leberman R. Polypeptide elongation factor Tu from Halobacterium marismortui. Eur J Biochem. 1988 Mar 15;172(3):687–694. doi: 10.1111/j.1432-1033.1988.tb13943.x. [DOI] [PubMed] [Google Scholar]
  7. Janin J. Surface and inside volumes in globular proteins. Nature. 1979 Feb 8;277(5696):491–492. doi: 10.1038/277491a0. [DOI] [PubMed] [Google Scholar]
  8. Jurnak F. Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Science. 1985 Oct 4;230(4721):32–36. doi: 10.1126/science.3898365. [DOI] [PubMed] [Google Scholar]
  9. Lanyi J. K. Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev. 1974 Sep;38(3):272–290. doi: 10.1128/br.38.3.272-290.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lechner J., Sumper M. The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem. 1987 Jul 15;262(20):9724–9729. [PubMed] [Google Scholar]
  11. Nagata S., Nagashima K., Tsunetsugu-Yokota Y., Fujimura K., Miyazaki M., Kaziro Y. Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae. EMBO J. 1984 Aug;3(8):1825–1830. doi: 10.1002/j.1460-2075.1984.tb02053.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Parker J. M., Guo D., Hodges R. S. New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry. 1986 Sep 23;25(19):5425–5432. doi: 10.1021/bi00367a013. [DOI] [PubMed] [Google Scholar]
  13. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Woese C. R., Olsen G. J. Archaebacterial phylogeny: perspectives on the urkingdoms. Syst Appl Microbiol. 1986;7:161–177. doi: 10.1016/s0723-2020(86)80001-7. [DOI] [PubMed] [Google Scholar]
  15. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]
  16. Yokota T., Sugisaki H., Takanami M., Kaziro Y. The nucleotide sequence of the cloned tufA gene of Escherichia coli. Gene. 1980 Dec;12(1-2):25–31. doi: 10.1016/0378-1119(80)90012-8. [DOI] [PubMed] [Google Scholar]
  17. Zaccai G., Cendrin F., Haik Y., Borochov N., Eisenberg H. Stabilization of halophilic malate dehydrogenase. J Mol Biol. 1989 Aug 5;208(3):491–500. doi: 10.1016/0022-2836(89)90512-3. [DOI] [PubMed] [Google Scholar]
  18. Zillig W., Palm P., Reiter W. D., Gropp F., Pühler G., Klenk H. P. Comparative evaluation of gene expression in archaebacteria. Eur J Biochem. 1988 May 2;173(3):473–482. doi: 10.1111/j.1432-1033.1988.tb14023.x. [DOI] [PubMed] [Google Scholar]
  19. la Cour T. F., Nyborg J., Thirup S., Clark B. F. Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO J. 1985 Sep;4(9):2385–2388. doi: 10.1002/j.1460-2075.1985.tb03943.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

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